2026-05-22T00:40:08Zhttps://repisalud.isciii.es/rest/oai/request

oai:repisalud.isciii.es:20.500.12105/188692024-11-29T22:01:44Zcom_20.500.12105_2173com_20.500.12105_2051col_20.500.12105_19597

00925njm 22002777a 4500 dc Chaves-Arquero, Belén author Martínez-Lumbreras, Santiago author Camero, Sergio author Santiveri, Clara M author Mirassou, Yasmina author Campos Olivas, Ramon author Jiménez, Maria Ángeles author Calvo, Olga author Pérez-Cañadillas, José Manuel author 2022-04 Heterodimerization of RNA binding proteins Nrd1 and Nab3 is essential to communicate the RNA recognition in the nascent transcript with the Nrd1 recognition of the Ser5-phosphorylated Rbp1 C-terminal domain in RNA polymerase II. The structure of a Nrd1-Nab3 chimera reveals the basis of heterodimerization, filling a missing gap in knowledge of this system. The free form of the Nrd1 interaction domain of Nab3 (NRID) forms a multi-state three-helix bundle that is clamped in a single conformation upon complex formation with the Nab3 interaction domain of Nrd1 (NAID). The latter domain forms two long helices that wrap around NRID, resulting in an extensive protein-protein interface that would explain the highly favorable free energy of heterodimerization. Mutagenesis of some conserved hydrophobic residues involved in the heterodimerization leads to temperature-sensitive phenotypes, revealing the importance of this interaction in yeast cell fitness. The Nrd1-Nab3 structure resembles the previously reported Rna14/Rna15 heterodimer structure, which is part of the poly(A)-dependent termination pathway, suggesting that both machineries use similar structural solutions despite they share little sequence homology and are potentially evolutionary divergent. Life Sci Alliance . 2022;5(4):e202101252. 10.26508/lsa.202101252 2575-1077 Life science alliance 35022249 http://hdl.handle.net/20.500.12105/18869 Structural basis of Nrd1-Nab3 heterodimerization.